BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 51782

Title: His6-AviTag-Sox2_aa234-317_C265A

Deposition date: 2023-01-10 Original release date: 2023-01-18

Authors: Theillet, Francois-Xavier

Citation: Theillet, Francois-Xavier. "Structural characterization of Oct4, Sox2, Nanog and Esrrb disordered domains, and a method to identify their phospho-dependent binding partners."  C. R. Chim. ., .-..

Assembly members:
entity_1, polymer, 112 residues, Formula weight is not available

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pet45b(+)

Entity Sequences (FASTA):
entity_1: MAHHHHHHVGTGLNDIFEAQ KIEWHEGAGMALGSMGSVVK SEASSSPPVVTSSSHSRAPA QAGDLRDMISMYLPGAEVPE PAAPSRLHMSQHYQSGPVPG TAINGTLPLSHM

Data sets:
Data typeCount
13C chemical shifts294
15N chemical shifts92
1H chemical shifts92

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1His6-AviTag-Sox2 aa234-317 C265A1

Entities:

Entity 1, His6-AviTag-Sox2 aa234-317 C265A 112 residues - Formula weight is not available

MAHHHHHHVGTGLNDIFEAQKIEWHEGA corresponds to His6-AviTag-, GMALGSMGSVVKSEASSSPPVVTSSSHSRAPAQAGDLRDMISMYLPGAEVPEPAAPSRLHMSQHYQSGPVPGTAINGTLPLSHM corresponds to human Sox2_aa234-317_C265A.

1   METALAHISHISHISHISHISHISVALGLY
2   THRGLYLEUASNASPILEPHEGLUALAGLN
3   LYSILEGLUTRPHISGLUGLYALAGLYMET
4   ALALEUGLYSERMETGLYSERVALVALLYS
5   SERGLUALASERSERSERPROPROVALVAL
6   THRSERSERSERHISSERARGALAPROALA
7   GLNALAGLYASPLEUARGASPMETILESER
8   METTYRLEUPROGLYALAGLUVALPROGLU
9   PROALAALAPROSERARGLEUHISMETSER
10   GLNHISTYRGLNSERGLYPROVALPROGLY
11   THRALAILEASNGLYTHRLEUPROLEUSER
12   HISMET

Samples:

sample_1: His6-AviTag-Sox2_aa234-317_C265A, [U-98% 13C; U-98% 15N], 600 ± 100 uM; DSS 0.1 mM; HEPES 20 mM; sodium chloride 50 mM; cocktail protease inhibitors 2 tablet/100mL

sample_conditions_1: ionic strength: 70 mM; pH: 6.8; pressure: 1 atm; temperature: 283 K

Experiments:

NameSampleSample stateSample conditions
1D 1Hsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D H(NCA)NHsample_1isotropicsample_conditions_1

Software:

TOPSPIN v3 - collection, processing

CcpNMR v2.1 - chemical shift assignment

NMR spectrometers:

  • Bruker Avance II 600 MHz

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts